Influence of receptors

Dorns RW (2000) Beyond receptor expression the influence of receptor conformation, density, and affinity in HlV-1 infection. Virology 276(2) 229-237 Dorns RW (2004) Unwelcome guests with master keys how HIV enters cells and how it can be stopped. Top HIV Med 12(4) 100-103... 

Doms RW. Beyond receptor expression the influence of receptor conformation, density, and affinity in HIV-1 infection. Virology 2000 276(2) 229-237. 

Influence of receptor axons on the formation of olfactory glomeruli in a hemimetabolous insect, the cockroach Periplaneta americana. Journal of Comparative Neurology 370 262-279. 

Cussac D, Newman-Tancredi A, Duqueyroix D, Pasteau V, Millan MJ. Differential activation of Gq/11 and Gi(3) proteins at 5-hydroxytryptamine(2C) receptors revealed by antibody capture assays influence of receptor reserve and relationship to agonist-directed trafficking. Mol Pharmacol 2002 62 578-589. 

Chan PY, Lawrence MB, Dustin ML, Eerguson LM, Golan DE, Springer TA. Influence of receptor lateral mohility on adhesion strengthening between membranes containing LEA-3 and CD2. J. Cell. Biol. 1991 115 245-255. 

Loutzenhiser, R and van Breemen, C. (1983). The influence of receptor occupation on Ca influx-mediated vascular smooth muscle contraction. Circ. Res. 1983 52 (suppl 1), 97-103. 

Binder, W.H., Kluger, C., Josipovic, M. et al. (2006) Directing supramolecular nanoparticle binding onto polymer films Film formation and influence of receptor density on binding densities. Macromolecules, 39,8092-8101. 

A typical force curve showing the specific avidin-biotin interaction is depicted in figure Bl.20.10. The SFA revealed the strong influence of hydration forces and membrane undulation forces on the specific binding of proteins to membrane-bound receptors [81]. 

Schuck P 1996 Kinetics of iigand binding to receptors immobiiized in a poiymer matrix, as detected with an evanescent wave biosensor, i. A computer simuiation of the influence of mass transport Biophys. J. 70 1230-49... 

Air pollutants reach receptors by being transported and perhaps transformed in the atmosphere (Fig. 18-1). The location of receptors relative to sources and atmospheric influences affect pollutant concentrations, and the sensitivity of receptors to these concentrations determines the effects. The location, height, and duration of release, as well as the amount of pollutant released, are also of importance. Some of the influences of the atmosphere on the behavior of pollutants, primarily the large-scale effects, are discussed here, as well as several effects of pollutants on the atmosphere. 

GPCR function has been shown to be regulated by several different mechanisms. The number of receptors on the plasma membrane may be regulated by transcription, mRNA stability, biosynthetic processing, and protein stability. In addition, the function of receptors in the plasma membrane can be influenced by regulatory phosphorylation and by association with other proteins that determine the subcellular location of receptors relative to other signaling molecules. 

Vitamin D3 (VD3) and retinoids synergistically inhibit the growth and progression of squamous cell carcinomas and actinic keratoses in chronically sun exposed skin. One reason for this synergism may be the direct influence of VD3 on the isomerization and the metabolism of RA. Here, VD3 inhibits the isomerization of 13-cis-RA to the more receptor active all-trans and 9-cis-isomers. Moreover, the VD3 derivative secocholestra-trien-l,3,24-triol (tacalcitol), used for the treatment of severe keratinizing disorders inhibits 4-hydroxylation of all-ri ans-RA. 

Similarly, in developing Drosophila the response to wg is influenced by the relative abundance and ligand affinity of receptors expressed in the target tissue. A synthesis of the available data from all species suggests that the response to a specific Wnt signal in vivo is influenced both by the particular Wnt protein secreted and by the receptors and other downstream molecules present in the target tissue. 

It is of interest that proteins termed motility factors (55-70 kD) are secreted by fetal cells and some tumor cells. These proteins act as autocrine factors and stimulate rapid movement by these cells. Motility factors induce the formation of cell processes that are packed with actin filaments and have an increased number of receptors for the matrix proteins laminin and fibronectin. The latter enhance the ability of the cells to bind to the extracellular matrix. Thus, it is likely that motility factors influence the organization of the cytoskeleton through changes taking place at the cell surface (reviewed by Warn and Dowrick, 1989). 

In the periphery at the mammalian neuromuscular junction each muscle fibre is generally influenced by only one nerve terminal and the one NT acts on one type of receptor localised to a specific (end-plate) area of the muscle. The system is fitted for the induction of the rapid short postsynaptie event of skeletal muscle fibre contraction and while the study of this synapse has been of immense value in elucidating some basic concepts of neurochemical transmission it would be unwise to use it as a universal template of synaptic transmission since it is atypical in many respects. 

In smooth muscle, by contrast, one sympathetic nerve fibre can influence a number of muscle fibres by releasing noradrenaline from varicosities along its length without there being any defined end-plate junctions. The result of receptor activation is a slow change in potential and inactivation of the NT is initially by uptake and then metabolism. In other words, the NT function is geared to the slower phasic changes in tone characteristic of smooth muscle. 

Krebs-Thomson, K, Paulus, MP and Geyer, MA (1998) Effects of hallucinogens on locomotor and investigatory activity and patterns influence of 5-HT2A and 5-HT2C receptors. Neuropsychopharmacology 18 339-351. 

Cao, BJ and Rodgers, RJ (1997) Influence of 5-HTia receptor antagonism on plus-maze behaviour in mice. II WAY 100635, SDZ 216-525 and NAN-190. Pharmacol. Biochem. Behav. 58 593-603. 

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